Intro to aa Flashcards

1
Q

Which two amino acids do not have a corresponding tranaminase?

A

T, K

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

What are the functions of transaminiases?

A

Tranform amino acids into their alpha-keto acids and back.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

What is required for all transaminase reactions?

A

Vitamin B6 (PLP)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

True or false, tranamination reactions are freely reversible

A

True

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

What is the precursor for alanine?

A

Pyruvate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Which reaction does ALT catalyze?

A

pyruvate to alanine (via E +aKG)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

What is a major reason ALT is important?

A

It allows muscles to transport pryruvate as an alanine to the liver during fasting. Pyruvate can then be used in gluconeogenesis.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

What is the enzyme AST used for?

A

To catalyze the reaction from OAA to D (via E/aKG)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

How is asparagine made?

A

From aspartate via ATP + E and asparagine synthase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Where is AST primarily found?

A

liver, cardiac and skeletal muscles, kidneys

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Where is ALT primarily found?

A

Liver –this is why it is diagnostic for liver damage.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

What does secretin cause the release of?

A

HCO3

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

What does cholecystokinin cause the release of?

A

Digestive enzymes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Which enzymes are activated by entreopeptidase?

A

Chymotripsin
Elastase
Carboxypeptidase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

What is the ratio of poly peptides to free amino acids after degradation by pancreatic proteases?

A

60/40

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Hartnup disease is the result of what? What are the symptoms? How is it treated>

A

Cannot uptake large, neutral amino acids
Results in pellegra due to no niacin
Treatment with niacin and large protein diet.

17
Q

Celiac disease is caused by an immune reaction to what part of gluten?

A

Alpha gliadin

18
Q

The body has how much free amino acids in the free amino acid pool?

A

100 g

19
Q

aKG and OAA are precursors to what amino acids?

A

PRENDQ

20
Q

pyruvate and 3PG are precursors for which amino acids?

A

AS

21
Q

Glutamate dehydroenase gets its amino group from where?

A

Free ammonium ion

22
Q

Glutamine synthetase gets its amino group from where?

A

Free ammonium ion

23
Q

ALT forms what from what

A

Alanine from Pyruvate

24
Q

Where does N get its amine from?

A

Q

25
Q

Homocysteine uria is a problem with what enzyme? Symptoms? Treatment?

A

Cystathione beta-synthase.
Lens dislocation, osteoporosis, MR, thromboembolism
Low M, high S diet,

26
Q

PKU is a problem with which two enzymes? Symptoms?

A

Either F-hydrolase or DHBtn reductase

MR, SZs, hypopigmentation